Origins of catalysis by computationally designed retroaldolase enzymes

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 11, 2010, Pages 4937-4942

  Lassila, Jonathan K ^a   Baker, David ^b   Herschlag, Daniel ^a  

^a STANFORD UNIVERSITY   (United States)

^b UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

Amine; Br nsted correlation; Catalytic mechanism; Computational enzyme design; Retroaldol reaction

Indexed keywords

AMINE; BRONSTED ACID; FRUCTOSE BISPHOSPHATE ALDOLASE; LYSINE; RETROALDOLASE ENZYME; UNCLASSIFIED DRUG; WATER;

ARTICLE; CATALYST; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME SPECIFICITY; HYDROPHOBICITY; MOLECULAR INTERACTION; MUTATIONAL ANALYSIS; PH; PRIORITY JOURNAL; PROTEIN MOTIF;

ALDEHYDES; AMINO ACID MOTIFS; BIOCATALYSIS; FRUCTOSE-BISPHOSPHATE ALDOLASE; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; KINETICS; LYSINE; MODELS, MOLECULAR; PROTEIN BINDING; SOLUTIONS; WATER;

EID: 77950437360     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0913638107     Document Type: Article

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